AURO_GIBZE
ID AURO_GIBZE Reviewed; 506 AA.
AC I1RF55;
DT 30-AUG-2017, integrated into UniProtKB/Swiss-Prot.
DT 13-JUN-2012, sequence version 1.
DT 03-AUG-2022, entry version 56.
DE RecName: Full=FAD-linked oxidoreductase aurO {ECO:0000303|PubMed:16879655};
DE EC=1.-.-.- {ECO:0000305};
DE AltName: Full=Aurofusarin biosynthesis cluster protein O {ECO:0000303|PubMed:16879655};
DE AltName: Full=Gibberella pigment protein 3 {ECO:0000303|PubMed:16461721};
GN Name=aurO {ECO:0000303|PubMed:16879655};
GN Synonyms=GIP3 {ECO:0000303|PubMed:16461721};
GN ORFNames=FG02321, FGRAMPH1_01T05587;
OS Gibberella zeae (strain ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084
OS / PH-1) (Wheat head blight fungus) (Fusarium graminearum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium.
OX NCBI_TaxID=229533;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1;
RX PubMed=17823352; DOI=10.1126/science.1143708;
RA Cuomo C.A., Gueldener U., Xu J.-R., Trail F., Turgeon B.G., Di Pietro A.,
RA Walton J.D., Ma L.-J., Baker S.E., Rep M., Adam G., Antoniw J., Baldwin T.,
RA Calvo S.E., Chang Y.-L., DeCaprio D., Gale L.R., Gnerre S., Goswami R.S.,
RA Hammond-Kosack K., Harris L.J., Hilburn K., Kennell J.C., Kroken S.,
RA Magnuson J.K., Mannhaupt G., Mauceli E.W., Mewes H.-W., Mitterbauer R.,
RA Muehlbauer G., Muensterkoetter M., Nelson D., O'Donnell K., Ouellet T.,
RA Qi W., Quesneville H., Roncero M.I.G., Seong K.-Y., Tetko I.V., Urban M.,
RA Waalwijk C., Ward T.J., Yao J., Birren B.W., Kistler H.C.;
RT "The Fusarium graminearum genome reveals a link between localized
RT polymorphism and pathogen specialization.";
RL Science 317:1400-1402(2007).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1;
RX PubMed=20237561; DOI=10.1038/nature08850;
RA Ma L.-J., van der Does H.C., Borkovich K.A., Coleman J.J., Daboussi M.-J.,
RA Di Pietro A., Dufresne M., Freitag M., Grabherr M., Henrissat B.,
RA Houterman P.M., Kang S., Shim W.-B., Woloshuk C., Xie X., Xu J.-R.,
RA Antoniw J., Baker S.E., Bluhm B.H., Breakspear A., Brown D.W.,
RA Butchko R.A.E., Chapman S., Coulson R., Coutinho P.M., Danchin E.G.J.,
RA Diener A., Gale L.R., Gardiner D.M., Goff S., Hammond-Kosack K.E.,
RA Hilburn K., Hua-Van A., Jonkers W., Kazan K., Kodira C.D., Koehrsen M.,
RA Kumar L., Lee Y.-H., Li L., Manners J.M., Miranda-Saavedra D.,
RA Mukherjee M., Park G., Park J., Park S.-Y., Proctor R.H., Regev A.,
RA Ruiz-Roldan M.C., Sain D., Sakthikumar S., Sykes S., Schwartz D.C.,
RA Turgeon B.G., Wapinski I., Yoder O., Young S., Zeng Q., Zhou S.,
RA Galagan J., Cuomo C.A., Kistler H.C., Rep M.;
RT "Comparative genomics reveals mobile pathogenicity chromosomes in
RT Fusarium.";
RL Nature 464:367-373(2010).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1;
RX PubMed=26198851; DOI=10.1186/s12864-015-1756-1;
RA King R., Urban M., Hammond-Kosack M.C.U., Hassani-Pak K.,
RA Hammond-Kosack K.E.;
RT "The completed genome sequence of the pathogenic ascomycete fungus Fusarium
RT graminearum.";
RL BMC Genomics 16:544-544(2015).
RN [4]
RP FUNCTION.
RX PubMed=15811992; DOI=10.1128/aem.71.4.1701-1708.2005;
RA Kim J.E., Han K.H., Jin J., Kim H., Kim J.C., Yun S.H., Lee Y.W.;
RT "Putative polyketide synthase and laccase genes for biosynthesis of
RT aurofusarin in Gibberella zeae.";
RL Appl. Environ. Microbiol. 71:1701-1708(2005).
RN [5]
RP FUNCTION, AND PATHWAY.
RX PubMed=15809006; DOI=10.1016/j.fgb.2005.01.010;
RA Malz S., Grell M.N., Thrane C., Maier F.J., Rosager P., Felk A.,
RA Albertsen K.S., Salomon S., Bohn L., Schaefer W., Giese H.;
RT "Identification of a gene cluster responsible for the biosynthesis of
RT aurofusarin in the Fusarium graminearum species complex.";
RL Fungal Genet. Biol. 42:420-433(2005).
RN [6]
RP FUNCTION, DISRUPTION PHENOTYPE, AND PATHWAY.
RX PubMed=16879655; DOI=10.1111/j.1365-2958.2006.05295.x;
RA Frandsen R.J., Nielsen N.J., Maolanon N., Soerensen J.C., Olsson S.,
RA Nielsen J., Giese H.;
RT "The biosynthetic pathway for aurofusarin in Fusarium graminearum reveals a
RT close link between the naphthoquinones and naphthopyrones.";
RL Mol. Microbiol. 61:1069-1080(2006).
RN [7]
RP INDUCTION.
RX PubMed=16461721; DOI=10.1128/aem.72.2.1645-1652.2006;
RA Kim J.E., Jin J., Kim H., Kim J.C., Yun S.H., Lee Y.W.;
RT "GIP2, a putative transcription factor that regulates the aurofusarin
RT biosynthetic gene cluster in Gibberella zeae.";
RL Appl. Environ. Microbiol. 72:1645-1652(2006).
RN [8]
RP FUNCTION, SUBCELLULAR LOCATION, SUBUNIT, AND PATHWAY.
RX PubMed=21296881; DOI=10.1074/jbc.m110.179853;
RA Frandsen R.J., Schuett C., Lund B.W., Staerk D., Nielsen J., Olsson S.,
RA Giese H.;
RT "Two novel classes of enzymes are required for the biosynthesis of
RT aurofusarin in Fusarium graminearum.";
RL J. Biol. Chem. 286:10419-10428(2011).
RN [9]
RP FUNCTION.
RX PubMed=23557488; DOI=10.1186/1475-2859-12-31;
RA Rugbjerg P., Naesby M., Mortensen U.H., Frandsen R.J.;
RT "Reconstruction of the biosynthetic pathway for the core fungal polyketide
RT scaffold rubrofusarin in Saccharomyces cerevisiae.";
RL Microb. Cell Fact. 12:31-31(2013).
CC -!- FUNCTION: FAD-linked oxidoreductase; part of the gene cluster that
CC mediates the biosynthesis of aurofusarin, a red mycelium pigment which
CC is acting as a mycotoxin (PubMed:15811992, PubMed:15809006,
CC PubMed:16879655). The first step is performed by the polyketide
CC synthase which condenses one acetyl-CoA and 6 malonyl-CoA units to form
CC the first intermediate, the cyclic heptaketide and yellow pigment YWA1
CC (PubMed:21296881, PubMed:23557488). The C2 hydroxyl group in the pyrone
CC ring of YWA1 is probably formed during ring closure by an aldol-type
CC cyclization reaction (PubMed:21296881). The dehydratase aurZ then acts
CC as the first tailoring enzyme in the aurofusarin biosynthetic pathway
CC by converting YWA1 to nor-rubrofusarin (PubMed:21296881,
CC PubMed:23557488). Nor-rubrofusarin is then methylated to rubrofusarin
CC by the O-methyltransferase aurJ (PubMed:21296881, PubMed:23557488).
CC Rubrofusarin is then transported across the plasma membrane by the
CC rubrofusarin-specific pump aurT for further enzymatic processing by the
CC extracellular complex composed of GIP1, aurF, aurO and aurS to yield
CC aurofusarin (PubMed:21296881). {ECO:0000269|PubMed:15809006,
CC ECO:0000269|PubMed:15811992, ECO:0000269|PubMed:16879655,
CC ECO:0000269|PubMed:21296881, ECO:0000269|PubMed:23557488}.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000250|UniProtKB:P08159};
CC -!- PATHWAY: Pigment biosynthesis. {ECO:0000269|PubMed:15809006,
CC ECO:0000269|PubMed:16879655, ECO:0000269|PubMed:21296881}.
CC -!- SUBUNIT: Might be part of an extracellular enzyme complex composed of
CC GIP1, aurF, aurO and aurS (PubMed:21296881).
CC {ECO:0000305|PubMed:21296881}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:21296881}. Secreted,
CC extracellular space {ECO:0000305|PubMed:21296881}.
CC -!- INDUCTION: Expression is regulated by the aurofusarin biosynthesis
CC cluster-specific transcription factor aurR1/GIP2 (PubMed:16461721).
CC {ECO:0000269|PubMed:16461721}.
CC -!- DISRUPTION PHENOTYPE: Impairs the production of aurofusarin and leads
CC to the accumulation of a light yellow pigment (PubMed:16879655).
CC {ECO:0000269|PubMed:16879655}.
CC -!- SIMILARITY: Belongs to the oxygen-dependent FAD-linked oxidoreductase
CC family. {ECO:0000305}.
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DR EMBL; HG970332; CEF74598.1; -; Genomic_DNA.
DR RefSeq; XP_011318230.1; XM_011319928.1.
DR AlphaFoldDB; I1RF55; -.
DR SMR; I1RF55; -.
DR STRING; 229533.I1RF55; -.
DR GeneID; 23549703; -.
DR KEGG; fgr:FGSG_02321; -.
DR VEuPathDB; FungiDB:FGRAMPH1_01G05587; -.
DR eggNOG; ENOG502SKWA; Eukaryota.
DR HOGENOM; CLU_018354_10_0_1; -.
DR InParanoid; I1RF55; -.
DR BioCyc; MetaCyc:MON-19452; -.
DR Proteomes; UP000070720; Chromosome 1.
DR GO; GO:0005615; C:extracellular space; IEA:UniProtKB-SubCell.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.30.43.10; -; 1.
DR Gene3D; 3.30.465.10; -; 1.
DR InterPro; IPR012951; BBE.
DR InterPro; IPR016166; FAD-bd_PCMH.
DR InterPro; IPR036318; FAD-bd_PCMH-like_sf.
DR InterPro; IPR016167; FAD-bd_PCMH_sub1.
DR InterPro; IPR016169; FAD-bd_PCMH_sub2.
DR InterPro; IPR006094; Oxid_FAD_bind_N.
DR Pfam; PF08031; BBE; 1.
DR Pfam; PF01565; FAD_binding_4; 1.
DR SUPFAM; SSF56176; SSF56176; 1.
DR PROSITE; PS51387; FAD_PCMH; 1.
PE 1: Evidence at protein level;
KW FAD; Flavoprotein; Oxidoreductase; Reference proteome; Secreted.
FT CHAIN 1..506
FT /note="FAD-linked oxidoreductase aurO"
FT /id="PRO_0000441091"
FT DOMAIN 92..260
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00718"
SQ SEQUENCE 506 AA; 54117 MW; B009B842CBB45FF5 CRC64;
MINSFSLFAH ITPIIRSSLH SRYSVISSRK AMSSLAAAPY RHVMMPFSPA QDAQVHGNSA
LTKLTDAIPD LKIYTRSSPH YESLRGVYNK LITAQPLAIC RPTSVAQVQA IVKTVSGLGI
PLGVRGGGHD VFGRGCIADS VTIDMRELDT QELSQDKKTV KVGGGITSKN LVGFLGSHNL
CTSNGFAGEA GWTSWASWGG YGPLGDYVGL GVDNIVGAKI VTASGDVVDA KGDSELLWAL
RGGGGNFGVI AETDVRVYPM STIQAGFIVY PWPETADVLL RLQALLDSGV PDKLCLQAGF
TKGEWGLGMA ITYIWPEAET IGPESEEWLQ KLKGLGTCIV DTVAETTFEA FQASISSAIS
NPVNVTSRHI SISKFTSDTL NQLIGACESM PAEADCSITC TILHGKAAQA NVLSAFGTRR
PHIMLHINAV TEEAAHEHVA IAWADRLVDG VEATGDSIGS TYVSFMESDK DPKGCYGENW
ERLKAVKKEV DPNDVFRFVH GRIPAA
